BMB Reports
- 제31권1호
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- Pages.20-24
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- 1998
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- 1976-670X(eISSN)
Characterization of Thioltransferase from Kale
- Sa, Jae-Hoon (Division of Life Science, College of Natural Science, Kangwon National University) ;
- Yong, Mi-Young (Division of Life Science, College of Natural Science, Kangwon National University) ;
- Song, Byung-Lim (Division of Life Science, College of Natural Science, Kangwon National University) ;
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Lim, Chang-Jin
(Division of Life Science, College of Natural Science, Kangwon National University)
- 발행 : 1998.01.31
초록
Thioltransferase, also known as glutaredoxin, is an enzyme that catalyzes the reduction of a variety of disulfides, including protein disulfides, in the presence of reduced glutathione. Thioltransferase was purified from kale through ammonium sulfate fractionation, DE-52 ion-exchange chromatography, Sephadex G-75 gel filtration, and Q-Sepharose ion-exchange chromatography. Its molecular size was estimated to be about 31,000 daltons on SDS-PAGE. The purified enzyme has an optimum pH of about 8.0 with 2-hydroxyethyl disulfide as a substrate. The enzyme also utilizes L-sulfocysteine, L-cystine, bovine serum albumin, and insulin as substrates in the presence of GSH. The enzyme has